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Imaging the structure and observing the dynamics of isolated proteins usingsingle-particle X-ray diffractive imaging (SPI) is one of the potentialapplications of X-ray free-electron lasers (XFELs). Currently, SPI experimentson isolated proteins are limited by three factors: low signal strength, limiteddata and high background from gas scattering. The last two factors are largelydue to the shortcomings of the aerosol sample delivery methods in use. Here wepresent our modified electrospray ionization (ESI) source, which we dubbedHelium-ESI (He-ESI). With it, we increased particle delivery into theinteraction region by a factor of 10, for 26 nm-sized biological particles, anddecreased the gas load in the interaction chamber corresponding to an 80%reduction in gas scattering when compared to the original ESI. Theseimprovements will lead to a significant increase in the quality and quantity ofSPI diffraction patterns in future experiments using He-ESI, resulting inhigher-resolution structures.

Helium-Electrospray: an improved sample delivery system for single-particle imaging with X-ray lasers